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P03188

- GB_EBVB9

UniProt

P03188 - GB_EBVB9

Protein

Envelope glycoprotein B

Gene

gB

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Envelope glycoprotein that forms spikes at the surface of virion envelope. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding of gp350/220 to its receptor, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei432 – 4332Cleavage; by host furinSequence Analysis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Envelope glycoprotein B
    Short name:
    gB
    Alternative name(s):
    GP115
    Glycoprotein GP110
    Gene namesi
    Name:gB
    ORF Names:BALF4
    OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
    Taxonomic identifieri10377 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007640: Genome

    Subcellular locationi

    Virion membrane By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity. Host endosome membrane By similarity; Single-pass type I membrane protein By similarity. Host Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity
    Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) By similarity.By similarity

    GO - Cellular componenti

    1. host cell endosome membrane Source: UniProtKB-SubCell
    2. host cell Golgi membrane Source: UniProtKB-SubCell
    3. host cell plasma membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. viral envelope Source: UniProtKB-KW
    6. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host endosome, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi112 – 1132WY → HR: Loss of fusion with epithelial cells. 1 Publication
    Mutagenesisi193 – 1964WLIW → RVEA: Loss of fusion with epithelial cells. 1 Publication
    Mutagenesisi428 – 4325RRRRR → DDDDK: Complete loss of proteolytic cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 857835Envelope glycoprotein BPRO_0000038190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 ↔ 528
    Disulfide bondi68 ↔ 484
    Glycosylationi76 – 761N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi141 ↔ 206
    Glycosylationi163 – 1631N-linked (GlcNAc...); by host1 Publication
    Glycosylationi290 – 2901N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi295 ↔ 342
    Glycosylationi329 – 3291N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi348 – 3481N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi436 – 4361N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi551 ↔ 588By similarity
    Glycosylationi563 – 5631N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi629 – 6291N-linked (GlcNAc...); by host1 Publication

    Post-translational modificationi

    A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.3 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotrimer; disulfide-linked.By similarity

    Protein-protein interaction databases

    DIPiDIP-47669N.
    MINTiMINT-6768112.

    Structurei

    Secondary structure

    1
    857
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi58 – 603
    Beta strandi77 – 8711
    Beta strandi92 – 11019
    Beta strandi115 – 12511
    Helixi129 – 1357
    Turni136 – 1383
    Beta strandi140 – 14910
    Beta strandi152 – 1576
    Helixi158 – 1603
    Beta strandi165 – 1673
    Beta strandi179 – 1835
    Beta strandi197 – 21519
    Beta strandi222 – 2243
    Beta strandi229 – 2324
    Turni248 – 2503
    Beta strandi251 – 2577
    Helixi262 – 2643
    Beta strandi272 – 2787
    Beta strandi283 – 2875
    Helixi291 – 2933
    Beta strandi296 – 31015
    Beta strandi315 – 3195
    Turni320 – 3234
    Beta strandi324 – 3296
    Helixi341 – 3433
    Helixi344 – 35613
    Turni357 – 3615
    Beta strandi362 – 3687
    Beta strandi370 – 3745
    Beta strandi379 – 3879
    Helixi458 – 49841
    Helixi502 – 5109
    Beta strandi516 – 5194
    Beta strandi522 – 5254
    Beta strandi533 – 5386
    Beta strandi556 – 5605
    Beta strandi567 – 5726
    Beta strandi576 – 5794
    Beta strandi593 – 5986
    Beta strandi601 – 6066
    Beta strandi609 – 6157
    Turni616 – 6183
    Helixi646 – 6505
    Helixi657 – 67317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FVCX-ray3.20A23-685[»]
    ProteinModelPortaliP03188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03188.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 732710Virion surfaceSequence AnalysisAdd
    BLAST
    Topological domaini754 – 857104IntravirionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei733 – 75321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni111 – 1144Involved in fusion and/or binding to host membraneSequence Analysis
    Regioni193 – 1975Involved in fusion and/or binding to host membraneSequence Analysis
    Regioni561 – 62060OligomerizationAdd
    BLAST
    Regioni709 – 72921Hydrophobic membrane proximal regionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi428 – 4325Poly-Arg
    Compositional biasi836 – 8394Poly-Arg

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR000234. Herpes_Glycoprot_B.
    [Graphical view]
    PfamiPF00606. Glycoprotein_B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P03188-1 [UniParc]FASTAAdd to Basket

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    MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV    50
    CELSSHGDLF RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT 100
    KIVTNILIYN GWYADSVTNR HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD 150
    GLTRVYVDRD GVNITVNLKP TGGLANGVRR YASQTELYDA PGWLIWTYRT 200
    RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN KETFHERADS 250
    FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW 300
    QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT 350
    MHEKYEAVQD RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT 400
    TPTSSPPSSP SPPAPSAARG STPAAVLRRR RRDAGNATTP VPPTAPGKSL 450
    GTLNNPATVQ IQFAYDSLRR QINRMLGDLA RAWCLEQKRQ NMVLRELTKI 500
    NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK SMRVPGSETM 550
    CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN 600
    EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR 650
    ASNVFDLEGI FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL 700
    GSVGQSITNL VSTVGGLFSS LVSGFISFFK NPFGGMLILV LVAGVVILVI 750
    SLTRRTRQMS QQPVQMLYPG IDELAQQHAS GEGPGINPIS KTELQAIMLA 800
    LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY HDPETAAALL 850
    GEAETEF 857
    Length:857
    Mass (Da):95,639
    Last modified:July 21, 1986 - v1
    Checksum:iD9BCE9487D8A1411
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01555 Genomic DNA. Translation: CAA24806.1.
    AJ507799 Genomic DNA. Translation: CAD53463.1.
    PIRiA03749. QQBE1L.
    RefSeqiYP_401713.1. NC_007605.1.

    Genome annotation databases

    GeneIDi3783680.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01555 Genomic DNA. Translation: CAA24806.1 .
    AJ507799 Genomic DNA. Translation: CAD53463.1 .
    PIRi A03749. QQBE1L.
    RefSeqi YP_401713.1. NC_007605.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FVC X-ray 3.20 A 23-685 [» ]
    ProteinModelPortali P03188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47669N.
    MINTi MINT-6768112.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3783680.

    Miscellaneous databases

    EvolutionaryTracei P03188.

    Family and domain databases

    InterProi IPR000234. Herpes_Glycoprot_B.
    [Graphical view ]
    Pfami PF00606. Glycoprotein_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus."
      Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.
      Mol. Biol. Med. 1:21-45(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB."
      Gong M., Ooka T., Matsuo T., Kieff E.
      J. Virol. 61:499-508(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF PROTEIN.
    4. Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
    5. "Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins."
      Backovic M., Leser G.P., Lamb R.A., Longnecker R., Jardetzky T.S.
      Virology 368:102-113(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 112-TRP-TYR-113; 193-TRP--TRP-196 AND 428-ARG--ARG-432, PROTEOLYTIC CLEAVAGE.
    6. "Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis."
      Reimer J.J., Backovic M., Deshpande C.G., Jardetzky T., Longnecker R.
      J. Virol. 83:734-747(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION REGION.
    7. "Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells."
      Sorem J., Longnecker R.
      J. Gen. Virol. 90:591-595(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE BY HOST FURIN.
    8. "Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B."
      Backovic M., Longnecker R., Jardetzky T.S.
      Proc. Natl. Acad. Sci. U.S.A. 106:2880-2885(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-685, GLYCOSYLATION AT ASN-163; ASN-290 AND ASN-629.

    Entry informationi

    Entry nameiGB_EBVB9
    AccessioniPrimary (citable) accession number: P03188
    Secondary accession number(s): Q777B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3